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  2. Cofactor (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Cofactor_(biochemistry)

    Coenzymes are further divided into two types. The first is called a "prosthetic group", which consists of a coenzyme that is tightly (or even covalently and, therefore, permanently) bound to a protein. [4] The second type of coenzymes are called "cosubstrates", and are transiently bound to the protein.

  3. Pyruvate decarboxylation - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_decarboxylation

    Energy-generating ions and molecules, such as amino acids and carbohydrates, enter the Krebs cycle as acetyl coenzyme A and oxidize in the cycle. [5] The pyruvate dehydrogenase complex (PDC) catalyzes the decarboxylation of pyruvate, resulting in the synthesis of acetyl-CoA, CO 2 , and NADH .

  4. Pyruvate dehydrogenase complex - Wikipedia

    en.wikipedia.org/wiki/Pyruvate_dehydrogenase_complex

    Pyruvate dehydrogenase complexes share many similarities with branched chain 2-oxoacid dehydrogenase (BCOADH), particularly in their substrate specificity for alpha-keto acids. Specifically, BCOADH catalyzes the degradation of amino acids and these enzymes would have been prevalent during the periods on prehistoric Earth dominated by rich amino ...

  5. Glycolysis - Wikipedia

    en.wikipedia.org/wiki/Glycolysis

    d -Glucose + 2 [NAD] + + 2 [ADP] + 2 [P] i 2 × Pyruvate 2 × + 2 [NADH] + 2 H + + 2 [ATP] + 2 H 2 O Glycolysis pathway overview The use of symbols in this equation makes it appear unbalanced with respect to oxygen atoms, hydrogen atoms, and charges. Atom balance is maintained by the two phosphate (P i) groups: Each exists in the form of a hydrogen phosphate anion, dissociating to contribute ...

  6. Dihydrolipoyl transacetylase - Wikipedia

    en.wikipedia.org/wiki/Dihydrolipoyl_transacetylase

    The first is thiamine pyrophosphate (TPP), which is used by pyruvate dehydrogenase to oxidize pyruvate and to form a hydroxyethyl-TPP intermediate. This intermediate is taken up by dihydrolipoyl transacetylase and reacted with a second lipoamide cofactor to generate an acetyl-dihydrolipoyl intermediate, releasing TPP in the process.

  7. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Since coenzymes are chemically changed as a consequence of enzyme action, it is useful to consider coenzymes to be a special class of substrates, or second substrates, which are common to many different enzymes. For example, about 1000 enzymes are known to use the coenzyme NADH. [63]

  8. Active site - Wikipedia

    en.wikipedia.org/wiki/Active_site

    [6]: 69 Coenzyme is a broad concept which includes metal ions, various vitamins and ATP. If an enzyme needs coenzyme to work itself, it is called an apoenzyme. In fact, it alone cannot catalyze reactions properly. Only when its cofactor comes in and binds to the active site to form holoenzyme does it work properly.

  9. Transamination - Wikipedia

    en.wikipedia.org/wiki/Transamination

    The amino group is accommodated by conversion of this coenzyme to pyridoxamine-5'-phosphate (PMP). PLP is covalently attached to the enzyme via a Schiff Base linkage formed by the condensation of its aldehyde group with the ε-amino group of an enzymatic Lys residue. The Schiff base, which is conjugated to the enzyme's pyridinium ring, is the ...